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The arms and legs are ceaselessly shaking, the muscles weaken and the movements are slower – all of the typical symptoms that many Parkinson's patients experience. The exact causes of this neurodegenerative disease are still unknown. In a recent study, a Swiss research team questions an already common understanding of the development of Parkinson's disease
Basel / Switzerland – Parkinson's disease was first described 200 years ago by a doctor British. Worldwide, more than six million people have Parkinson's disease. In patients, dopaminergic nerve cells die slowly in the brain. The resultant shortage of this messenger alters motor skills and often cognitive abilities. The exact causes of the neurodegenerative disease are still unknown.
Does the protein fibrils of alpha-synuclein cause Parkinson's disease?
Previously, it was thought that one of the triggers was the alpha-synuclein protein. It can agglutinate and deposit itself as Lewy bodies in nerve cells. Toxic protein fibers are the basis of brain cells. A research team led by Professor Henning Stahlberg of the Biozentrum of the University of Basel collaborated with researchers from Hoffmann-La Roche Ltd. and ETH Zurich thus artificially generated an alpha-synuclein fibril in a reagent container and made it visible for the first time at an atomic resolution. "Contrary to our expectations, however, the results raise more questions than they answer," says Stahlberg.
It should be noted that in some congenital forms of Parkinson's disease, individuals with genetic disorders of the alpha-synuclein gene. Mutations, it is believed, eventually lead to incorrect protein folding and assembly in dangerous fibrils.
"However, our three-dimensional structure shows a fibrillar structure that could not be formed with such a mutated protein," says Stahlberg. "Most of these mutations, because of their location, would hinder the formation of the fibrillar structure we found." In short, if this fibrillar structure were to trigger Parkinson's disease, then the gene defect should protect against disease. But he does not do it. It could be that another form of fibrils or another form of the protein triggers the disease in these patients.
A study raises new questions about the development of Parkinson's disease
. What are the causes of mutations of alpha-synuclein, the formation of other aggregates of proteins, the role of fibrils in nerve cells? The questions must now be studied. To date, the exact function of alpha-synuclein is not clear. Since only symptoms can be relieved with the previous medication, new concepts are urgently needed.
Original article : Ricardo Guerrero-Ferreira, Nicholas M.I. Taylor, Daniel Mona, Philippe Ringler, Matthias E. Lauer, Roland Riek, Markus Britschgi and Henning Stahlberg. Cryo-EM structure of alpha-synuclein fibrils, eLife, published online July 3, 2018, doi: 10.7554 / eLife.36402
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